1oeu

From Proteopedia

(Difference between revisions)

Revision as of 04:56, 10 September 2015

Oxidation state of protein tyrosine phosphatase 1B

Structural highlights

1oeu is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1a5y, 1aax, 1bzc, 1bzh, 1bzj, 1c83, 1c84, 1c85, 1c86, 1c87, 1c88, 1ecv, 1een, 1eeo, 1g1f, 1g1g, 1g1h, 1g7f, 1g7g, 1gfy, 1i57, 1jf7, 1kak, 1kav, 1l8g, 1lqf, 1n6w, 1oem, 1oeo, 1oes, 1oet, 1oev, 1ptt, 1ptu, 1ptv, 1pty, 2hnp, 2hnq
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PTN1_HUMAN] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Protein tyrosine phosphatases regulate signal transduction pathways involving tyrosine phosphorylation and have been implicated in the development of cancer, diabetes, rheumatoid arthritis and hypertension. Increasing evidence suggests that the cellular redox state is involved in regulating tyrosine phosphatase activity through the reversible oxidization of the catalytic cysteine to sulphenic acid (Cys-SOH). But how further oxidation to the irreversible sulphinic (Cys-SO2H) and sulphonic (Cys-SO3H) forms is prevented remains unclear. Here we report the crystal structures of the regulatory sulphenic and irreversible sulphinic and sulphonic acids of protein tyrosine phosphatase 1B (PTP1B), an important enzyme in the negative regulation of the insulin receptor and a therapeutic target in type II diabetes and obesity. We also identify a sulphenyl-amide species that is formed through oxidation of its catalytic cysteine. Formation of the sulphenyl-amide causes large changes in the PTP1B active site, which are reversible by reduction with the cellular reducing agent glutathione. The sulphenyl-amide is a protective intermediate in the oxidative inhibition of PTP1B. In addition, it may facilitate reactivation of PTP1B by biological thiols and signal a unique state of the protein.

Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B.,van Montfort RL, Congreve M, Tisi D, Carr R, Jhoti H Nature. 2003 Jun 12;423(6941):773-7. PMID:12802339^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nievergall E, Janes PW, Stegmayer C, Vail ME, Haj FG, Teng SW, Neel BG, Bastiaens PI, Lackmann M. PTP1B regulates Eph receptor function and trafficking. J Cell Biol. 2010 Dec 13;191(6):1189-203. doi: 10.1083/jcb.201005035. Epub 2010, Dec 6. PMID:21135139 doi:10.1083/jcb.201005035
↑ Krishnan N, Fu C, Pappin DJ, Tonks NK. H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci Signal. 2011 Dec 13;4(203):ra86. doi: 10.1126/scisignal.2002329. PMID:22169477 doi:10.1126/scisignal.2002329
↑ van Montfort RL, Congreve M, Tisi D, Carr R, Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature. 2003 Jun 12;423(6941):773-7. PMID:12802339 doi:10.1038/nature01681

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oeu"

@@ Line 7: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a5y|1a5y]], [[1aax|1aax]], [[1bzc|1bzc]], [[1bzh|1bzh]], [[1bzj|1bzj]], [[1c83|1c83]], [[1c84|1c84]], [[1c85|1c85]], [[1c86|1c86]], [[1c87|1c87]], [[1c88|1c88]], [[1ecv|1ecv]], [[1een|1een]], [[1eeo|1eeo]], [[1g1f|1g1f]], [[1g1g|1g1g]], [[1g1h|1g1h]], [[1g7f|1g7f]], [[1g7g|1g7g]], [[1gfy|1gfy]], [[1i57|1i57]], [[1jf7|1jf7]], [[1kak|1kak]], [[1kav|1kav]], [[1l8g|1l8g]], [[1lqf|1lqf]], [[1n6w|1n6w]], [[1oem|1oem]], [[1oeo|1oeo]], [[1oes|1oes]], [[1oet|1oet]], [[1oev|1oev]], [[1ptt|1ptt]], [[1ptu|1ptu]], [[1ptv|1ptv]], [[1pty|1pty]], [[2hnp|2hnp]], [[2hnq|2hnq]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oeu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oeu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oeu RCSB], [http://www.ebi.ac.uk/pdbsum/1oeu PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oeu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oeu OCA], [http://pdbe.org/1oeu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oeu RCSB], [http://www.ebi.ac.uk/pdbsum/1oeu PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1oeu" style="background-color:#fffaf0;"></div>
 ==See Also==

1oeu

From Proteopedia

Revision as of 04:56, 10 September 2015

Oxidation state of protein tyrosine phosphatase 1B

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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